Available reactivities

Available hosts

Available applications

Background of Glutamate receptor 5 / GLUR5 antibody

L-Glutamate, the major excitatory neurotransmitter in the central nervous system (CNS), operates through several receptors that are categorized as ionotropic (ligand-gated cation channels) or metabotropic (G-protein-coupled receptors). The ligand-gated ion channel family consists of fifteen members that have been subdivided into three families based upon their pharmacological profile: the α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA)-preferring receptors, the N-methyl-D-aspartate (NMDA)-preferring receptors, and the kaite-preferring receptors. The kaite receptor subfamily consists of five members that have been further subdivided into two classes based upon structural homology and functiol characteristics. GluR5, GluR6, and GluR7receptor subunits share a high degree of homology and are able to form functiol channels when expressed in heterologous systems. The KA-1 and KA-2 receptors are uble to form functiol channels on their own, but when coexpressed with GluR5-7 receptor subunits, they form channels with high affinity for kaite. Like AMPA receptors, the functiol unit of endogenous kaite receptors is believed to be a tetramer, which can be either homomeric or heteromeric. Kaite receptors GluR5 and GluR6 (but not GluR7, KA-1, or KA-2) can undergo R editing; as in the AMPA receptor GluR2, a glutamine (Q) residue in the channel pore is edited to encode arginine (R) in the mature protein. Substitution of Q with R modulates the properties of the channel, producing channels with reduced single channel conductance and lower permeability to Ca2+. GluR5 is highly expressed in dorsal root ganglion (DRG) neurons of the peripheral nervous system (PNS) as well as in several structures of the CNS including the amygdala, the hipoccampus, and Purkinje cells of the cerebellum. GluR5 has been implicated in the modulation of syptic transmission and syptic plasticity in both the CNS and PNS, but the exact physiological function of GluR5 is not well understood. Nevertheless, an involvement in persistent pain and some types of learning has been proposed.